MolNFT v1 · #66369 · protein

Crystal structure of the thermus thermophilus M32 carboxypeptidase

3HOA · Thermostable carboxypeptidase 1: “Crystal structure of the thermus thermophilus M32 carboxypeptidase”. X-ray diffraction, 10 pockets (best druggability 0.76). MolNFT v1 #66369 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 3HOA
Type: protein
Length: 1,018 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thermostable carboxypeptidase 1
EC: 3.4.17.19
UniProt: Q72GY3
Pockets: 10 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 68% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thermostable carboxypeptidase 1 (EC 3.4.17.19)	protein	509	68% helix, 4% strand	Q72GY3

Ligands and binding sites

GOL · Glycerol · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	614	0.76	0.82	59	empty
2	784	0.74	0.79	68	empty
3	851	0.73	0.78	67	empty
4	621	0.73	0.80	75	empty
5	164	0.53	0.79	21	empty

Interfaces

1 interface between chains.

A–B · 1589 Å² buried · 30 hydrogen bonds · protein-protein

Compared structures

3HOA · Crystal structure of the Thermus thermophilus M32 carboxypeptidase · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q72GY3
Elsewhere: RCSB PDB 3HOA · PDBe 3HOA · UniProt Q72GY3

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